Summary for 6IGC
| Entry DOI | 10.2210/pdb6igc/pdb |
| Descriptor | Major capsid protein L1 (1 entity in total) |
| Functional Keywords | capsid protein, structural protein |
| Biological source | Human papillomavirus type 58 |
| Total number of polymer chains | 40 |
| Total formula weight | 2365772.04 |
| Authors | |
| Primary citation | Li, Z.,Song, S.,He, M.,Wang, D.,Shi, J.,Liu, X.,Li, Y.,Chi, X.,Wei, S.,Yang, Y.,Wang, Z.,Li, J.,Qian, H.,Yu, H.,Zheng, Q.,Yan, X.,Zhao, Q.,Zhang, J.,Gu, Y.,Li, S.,Xia, N. Rational design of a triple-type human papillomavirus vaccine by compromising viral-type specificity. Nat Commun, 9:5360-5360, 2018 Cited by PubMed Abstract: Sequence variability in surface-antigenic sites of pathogenic proteins is an important obstacle in vaccine development. Over 200 distinct genomic sequences have been identified for human papillomavirus (HPV), of which more than 18 are associated with cervical cancer. Here, based on the high structural similarity of L1 surface loops within a group of phylogenetically close HPV types, we design a triple-type chimera of HPV33/58/52 using loop swapping. The chimeric VLPs elicit neutralization titers comparable with a mix of the three wild-type VLPs both in mice and non-human primates. This engineered region of the chimeric protein recapitulates the conformational contours of the antigenic surfaces of the parental-type proteins, offering a basis for this high immunity. Our stratagem is equally successful in developing other triplet-type chimeras (HPV16/35/31, HPV56/66/53, HPV39/68/70, HPV18/45/59), paving the way for the development of an improved HPV prophylactic vaccine against all carcinogenic HPV strains. This technique may also be extrapolated to other microbes. PubMed: 30560935DOI: 10.1038/s41467-018-07199-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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